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O00086

- IMDH_CANAX

UniProt

O00086 - IMDH_CANAX

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Protein

Inosine-5'-monophosphate dehydrogenase

Gene
IMH3, IMD3
Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.1 Publication

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

Potassium By similarity.UniRule annotation

Enzyme regulationi

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. Potently inhibited by MPA.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi328 – 3281Potassium; via carbonyl oxygen By similarity
Metal bindingi330 – 3301Potassium; via carbonyl oxygen By similarity
Binding sitei331 – 3311IMP By similarity
Active sitei333 – 3331Thioimidate intermediate By similarity
Metal bindingi333 – 3331Potassium; via carbonyl oxygen By similarity
Binding sitei447 – 4471IMP By similarity
Metal bindingi506 – 5061Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi507 – 5071Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi276 – 2783NAD By similarity
Nucleotide bindingi326 – 3283NAD By similarity

GO - Molecular functioni

  1. adenyl nucleotide binding Source: InterPro
  2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. GMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

UniPathwayiUPA00601; UER00295.

Names & Taxonomyi

Protein namesi
Recommended name:
Inosine-5'-monophosphate dehydrogenase (EC:1.1.1.205)
Short name:
IMP dehydrogenase
Short name:
IMPD
Short name:
IMPDH
Gene namesi
Name:IMH3
Synonyms:IMD3
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Organism-specific databases

CGDiCAL0000509. IMH3.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Inosine-5'-monophosphate dehydrogenaseUniRule annotationPRO_0000093685Add
BLAST

2D gel databases

COMPLUYEAST-2DPAGEO00086.

Expressioni

Developmental stagei

Expressed at equal levels in the yeast or hyphal form.UniRule annotation

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi5476.CAL0000509.

Structurei

3D structure databases

ProteinModelPortaliO00086.
SMRiO00086. Positions 9-519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 17860CBS 1Add
BLAST
Domaini182 – 23857CBS 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 3683IMP binding By similarity
Regioni389 – 3902IMP binding By similarity
Regioni413 – 4175IMP binding By similarity

Sequence similaritiesi

Belongs to the IMPDH/GMPR family.
Contains 2 CBS domains.

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
PhylomeDBiO00086.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01964. IMPDH.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
PfamiPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000130. IMPDH. 1 hit.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
PROSITEiPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00086-1 [UniParc]FASTAAdd to Basket

« Hide

MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP    50
SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC 100
TSEEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMGE VLGFTSFPVT 150
ENGKVGGKLV GIITSRDIQF HEDNKSPVSE VMTKDLVVGK KGISLTDGNE 200
LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA 250
AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ 300
VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY 350
GVTEFANKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG 400
DYFYRDGKRL KTYRGMGSID AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS 450
GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRENVD NGEIRFEFRT 500
ASAQFEGGVH GLHSYEKRLH N 521
Length:521
Mass (Da):56,239
Last modified:July 1, 1997 - v1
Checksum:i5F1E52611B1E1418
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85049 Genomic DNA. Translation: AAB51509.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85049 Genomic DNA. Translation: AAB51509.1 .

3D structure databases

ProteinModelPortali O00086.
SMRi O00086. Positions 9-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5476.CAL0000509.

2D gel databases

COMPLUYEAST-2DPAGE O00086.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

CGDi CAL0000509. IMH3.

Phylogenomic databases

eggNOGi COG0517.
PhylomeDBi O00086.

Enzyme and pathway databases

UniPathwayi UPA00601 ; UER00295 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01964. IMPDH.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view ]
PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
Pfami PF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000130. IMPDH. 1 hit.
SMARTi SM00116. CBS. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
PROSITEi PS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Overexpression of a cloned IMP dehydrogenase gene of Candida albicans confers resistance to the specific inhibitor mycophenolic acid."
    Koehler G.A., White T.C., Agabian N.
    J. Bacteriol. 179:2331-2338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION.
    Strain: SS.

Entry informationi

Entry nameiIMDH_CANAX
AccessioniPrimary (citable) accession number: O00086
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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